人 TIMM9 抗体对
01AB03265
Translocase of inner mitochondrial membrane 9 (TIMM9) is a highly conserved mitochondrial intermembrane space chaperone that forms heterooligomeric complexes, primarily with TIMM10, to facilitate the import and insertion of multi-pass transmembrane proteins into the inner mitochondrial membrane. Structurally, TIMM9 contains a central loop flanked by disulfide bonds, separating extended N- and C-terminal helices, and assembles into hexameric complexes that stabilize and guide hydrophobic precursor proteins, preventing their aggregation during translocation. It is essential for the viability of eukaryotic cells, as it mediates the transfer of carrier proteins from the TOM complex to the SAM complex and is tightly associated with the TIM22 import machinery. Recent studies suggest its dysregulation may serve as a prognostic biomarker in multiple cancers, implicating altered mitochondrial protein import in tumorigenesis.
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技术参数
- 靶点基因名
- TIMM9
- 基因别名
- TIM9; TIM9A; TIMM9A
- 蛋白别名
- translocase of inner mitochondrial membrane 9; TIMM9
- UniProt
- Q9Y5J7
- 物种
- Human
产品详情
- 靶点名称
- TIMM9
- 蛋白名称
- translocase of inner mitochondrial membrane 9
- 蛋白别名
- Mitochondrial import inner membrane translocase subunit Tim9
- 靶点基因名
- TIMM9
- 基因别名
- TIM9; TIM9A; TIMM9A
- UniProt
- Q9Y5J7
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Translocase of inner mitochondrial membrane 9 (TIMM9) is a highly conserved mitochondrial intermembrane space chaperone that forms heterooligomeric complexes, primarily with TIMM10, to facilitate the import and insertion of multi-pass transmembrane proteins into the inner mitochondrial membrane. Structurally, TIMM9 contains a central loop flanked by disulfide bonds, separating extended N- and C-terminal helices, and assembles into hexameric complexes that stabilize and guide hydrophobic precursor proteins, preventing their aggregation during translocation. It is essential for the viability of eukaryotic cells, as it mediates the transfer of carrier proteins from the TOM complex to the SAM complex and is tightly associated with the TIM22 import machinery. Recent studies suggest its dysregulation may serve as a prognostic biomarker in multiple cancers, implicating altered mitochondrial protein import in tumorigenesis.